The studies herein proposed aim to define the composition of regulatory, structural and mechanochemical protein systems, and their involvement in synaptosomal functions, i.e., the storage, release and uptake of neurotransmitters. Contractile, regulatory and endocytotic brain proteins depend on calcium to perform their functions, in a fashion similar to the regulatory proteins of striated muscle and non-muscle tissues. In brain, however, individual components of the contractile and mechanochemical regulatory systems may be found in discrete locations in the nerve-ending wherein clathrin co-exists with alpha-actinin on vesicles while interacting with actin/tropomyosin complexes associated with the synaptosomal membrane. The lattice protein (clathrin) seems involved recycling membranes, macro-molecules and neurotransmitters. The regulated assembly of clathrin into a lattice or coat around vesicles permits a microfilamentous network to produce an organized movement of packaged neurotransmitters for metabolic activation and eventual release at the synaptosomal junction. These activities are turned off when the divalent cation/nucleotide complexes are sequestered either by specific proteins and/or organelles in vitro and in vivo. This study plans to define these regulatory, mechanochemical and endocytotic activities in synaptosomes by determining the interaction between individual protein components of each system and organelles in the synaptosome. Our purified antibodies will be used to establish their localization and the common structural parameters shared by these proteins. Our long-range goal is to try our experimental approach on specimens from deceased subjects having known neurological disorders.